{"id":"3dde6284-480a-5f7d-9fb7-fbe0fd59aa65","stable_key":"research:selenos-supports-erad","predicate":"supports_in_tested_model","statement":"SELENOS-p97 interaction contributes to degradation of the ERAD substrate tested in the mutational study.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"literature_reviewed:supported_interpretation","direction":"positive","is_public":true,"mechanism_event_id":"36ff6376-b243-50b2-86e2-946021a89450","mechanism_event_label":"The SELENOS-p97 connection helps dispose of a tested faulty protein.","subject":{"id":"969b7b10-229c-5dd5-b4c1-0ebef0bc0321","slug":"selenos","display_name":"SELENOS","entity_type_key":"protein"},"object":{"id":"630593e5-1447-55a0-b116-dcd5b6114672","slug":"erad","display_name":"ERAD","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"36ff6376-b243-50b2-86e2-946021a89450","stable_key":"research:selenos-supports-erad","event_type":"experimentally_scoped_interaction","label":"The SELENOS-p97 connection helps dispose of a tested faulty protein.","description":"SELENOS-p97 interaction contributes to degradation of the ERAD substrate tested in the mutational study.","status":"active","compartment":{"slug":"endoplasmic-reticulum","display_name":"Endoplasmic reticulum"},"participants":[{"entity":{"id":"969b7b10-229c-5dd5-b4c1-0ebef0bc0321","slug":"selenos","display_name":"SELENOS","entity_type_key":"protein"},"role":"regulator","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"630593e5-1447-55a0-b116-dcd5b6114672","slug":"erad","display_name":"ERAD","entity_type_key":"cellular_process"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"274ba2bf-699a-5e3a-aa0b-b6d290e37c7e","slug":"vcp","display_name":"VCP/p97","entity_type_key":"protein"},"role":"binding_partner","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"experimental_model","value_text":"Cultured-cell SELENOS mutation, protein-interaction and degradation assays.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Do not generalize one substrate assay to every ERAD substrate or assume dietary deficiency reproduces a binding-site mutation.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"organism","value_text":"Cultured mammalian cells","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"a04ca438-ab3d-526c-ab5d-2d7d03549e47","evidence_kind":"curated_literature_summary","locator":"lines 1086-1095","start_line":1086,"end_line":1095,"excerpt":"## selenos-supports-erad\n\nThe SELENOS-p97 connection helps dispose of a tested faulty protein.\n\nSELENOS-p97 interaction contributes to degradation of the ERAD substrate tested in the mutational study.\n\nExperimental model: Cultured-cell SELENOS mutation, protein-interaction and degradation assays.\nOrganism: Cultured mammalian cells\nLimitations: Do not generalize one substrate assay to every ERAD substrate or assume dietary deficiency reproduces a binding-site mutation.\nPrimary reference: [Pro178 and Pro183 of Selenoprotein S Are Essential Residues for Interaction with p97 during ER-associated Degradation](https://pmc.ncbi.nlm.nih.gov/articles/PMC4022850/)","model_system":"Cultured-cell SELENOS mutation, protein-interaction and degradation assays.","directness":"author_interpretation","verification_status":"secondary_verified","notes":"Curated summary; inspect the linked primary papers for original methods and results.","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"4f892f13-06ea-5199-a33c-a703f35c80ae","stable_key":"selenium-research-2026-09-17","title":"Selenium: literature corrections and mechanism additions","document_type":"curated_literature_review","citation_label":"Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually","file_path":"","sha256":"0b818b10c1c7120e5caf7f4d4019d7bd025d745692e424f515d3ef903c9ab7f3","revision_id":"80984e03-5f0f-5877-8094-afef7637444e","review_status":"secondary_verified","notes":"Secondary curated summaries of primary experiments, with explicit models and limitations. Not archived primary full text."}}],"relations":[],"conflicts":[],"corrections":[],"research":{"topic":"Protein folding","plain_language":"The SELENOS-p97 connection helps dispose of a tested faulty protein.","evidence_scope":"supported_interpretation","papers":[{"key":"catalog-selenos-2014","title":"Pro178 and Pro183 of Selenoprotein S Are Essential Residues for Interaction with p97 during ER-associated Degradation","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC4022850/","doi":null,"year":2014,"model":"Cultured-cell SELENOS mutation, protein-interaction and degradation assays.","summary":"Specific SELENOS proline substitutions disrupted p97 binding and the tested ERAD function."}]}}